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SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)

 SH2B1_MOUSE             Reviewed;         756 AA.
Q91ZM2; O54867; Q05DJ7; Q792R7; Q91ZM3; Q91ZV5; Q9WVM5;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
17-JUN-2020, entry version 139.
RecName: Full=SH2B adapter protein 1;
AltName: Full=Pro-rich, PH and SH2 domain-containing signaling mediator;
Short=PSM;
AltName: Full=SH2 domain-containing protein 1B;
AltName: Full=SH2-B PH domain-containing signaling mediator 1;
Name=Sh2b1; Synonyms=Sh2bpsm1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
INTERACTION WITH INSR.
PubMed=9498552; DOI=10.1093/oxfordjournals.jbchem.a021868;
Riedel H., Wang J., Hansen H., Yousaf N.;
"PSM, an insulin-dependent, pro-rich, PH, SH2 domain containing partner of
the insulin receptor.";
J. Biochem. 122:1105-1113(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), ALTERNATIVE SPLICING (ISOFORMS 1; 2
AND 3), TISSUE SPECIFICITY, AND INTERACTION WITH INSR AND ISR1.
PubMed=10594240; DOI=10.1007/s003359901183;
Nelms K., O'Neill T.J., Li S., Hubbard S.R., Gustafson T.A., Paul W.E.;
"Alternative splicing, gene localization, and binding of SH2-B to the
insulin receptor kinase domain.";
Mamm. Genome 10:1160-1167(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, AND
PHOSPHORYLATION.
TISSUE=Brain;
PubMed=11502739; DOI=10.1074/jbc.m104191200;
Yousaf N., Deng Y., Kang Y., Riedel H.;
"Four PSM/SH2-B alternative splice variants and their differential roles in
mitogenesis.";
J. Biol. Chem. 276:40940-40948(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 518-631, AND INTERACTION WITH INSR AND IGF1R.
PubMed=9452421; DOI=10.1074/jbc.273.6.3136;
Wang J., Riedel H.;
"Insulin-like growth factor-I receptor and insulin receptor association
with a Src homology-2 domain-containing putative adapter.";
J. Biol. Chem. 273:3136-3139(1998).
[7]
FUNCTION IN GH SIGNALING, AND INTERACTION WITH JAK2.
TISSUE=Kidney;
PubMed=9343427; DOI=10.1128/mcb.17.11.6633;
Rui L., Mathews L.S., Hotta K., Gustafson T.A., Carter-Su C.;
"Identification of SH2-Bbeta as a substrate of the tyrosine kinase JAK2
involved in growth hormone signaling.";
Mol. Cell. Biol. 17:6633-6644(1997).
[8]
FUNCTION IN LEPTIN SIGNALING, AND INTERACTION WITH JAK2; ISR1 AND ISR2.
PubMed=15316008; DOI=10.1074/jbc.m408495200;
Duan C., Li M., Rui L.;
"SH2-B promotes insulin receptor substrate 1 (IRS1)- and IRS2-mediated
activation of the phosphatidylinositol 3-kinase pathway in response to
leptin.";
J. Biol. Chem. 279:43684-43691(2004).
[9]
FUNCTION IN LEPTIN SIGNALING.
PubMed=16098827; DOI=10.1016/j.cmet.2005.07.004;
Ren D., Li M., Duan C., Rui L.;
"Identification of SH2-B as a key regulator of leptin sensitivity, energy
balance, and body weight in mice.";
Cell Metab. 2:95-104(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-96; SER-417 AND
SER-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[12]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-270, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 519-627 IN COMPLEX WITH JAK2.
PubMed=16824542; DOI=10.1016/j.jmb.2006.05.070;
Hu J., Hubbard S.R.;
"Structural basis for phosphotyrosine recognition by the Src homology-2
domains of the adapter proteins SH2-B and APS.";
J. Mol. Biol. 361:69-79(2006).
-!- FUNCTION: Adapter protein for several members of the tyrosine kinase
receptor family. Involved in multiple signaling pathways mediated by
Janus kinase (JAK) and receptor tyrosine kinases, including the
receptors of insulin (INS), insulin-like growth factor I (IGF1), nerve
growth factor (NGF), brain-derived neurotrophic factor (BDNF), glial
cell line-derived neurotrophic factor (GDNF), platelet-derived growth
factor (PDGF) and fibroblast growth factors (FGFs). In growth hormone
(GH) signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1,
which in turn is phosphorylated by JAK2 on tyrosine residues. These
phosphotyrosines form potential binding sites for other signaling
proteins. GH also promotes serine/threonine phosphorylation of SH2B1
and these phosphorylated residues may serve to recruit other proteins
to the GHR-JAK2-SH2B1 complexes, such as RAC1. In leptin (LEP)
signaling, binds to and potentiates the activation of JAK2 by globally
enhancing downstream pathways. In response to leptin, binds
simultaneously to both, JAK2 and IRS1 or IRS2, thus mediating formation
of a complex of JAK2, SH2B1 and IRS1 or IRS2. Mediates tyrosine
phosphorylation of IRS1 and IRS2, resulting in activation of the PI 3-
kinase pathway. Acts as positive regulator of NGF-mediated activation
of the Akt/Forkhead pathway; prolongs NGF-induced phosphorylation of
AKT1 on 'Ser-473' and AKT1 enzymatic activity. Enhances the kinase
activity of the cytokine receptor-associated tyrosine kinase JAK2 and
of other receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2,
the mechanism seems to involve dimerization of both, SH2B1 and JAK2.
Enhances RET phosphorylation and kinase activity (By similarity).
Isoforms seem to be differentially involved in IGF-I and PDGF-induced
mitogenesis, according the order: isoform 3 > isoform 4 > isoform 1 >
isoform 2. {ECO:0000250, ECO:0000269|PubMed:11502739,
ECO:0000269|PubMed:15316008, ECO:0000269|PubMed:16098827,
ECO:0000269|PubMed:9343427}.
-!- SUBUNIT: Self-associates. Homopentamer (By similarity). Forms a
heteromultimeric complex with SH2B2 (By similarity). Interacts with
SH2B2. Isoform 1 interacts via its SH2 domain with JAK2. Isoform 2
interacts via its SH2 domain and its N-terminus with JAK2; the SH2
domain is required for the major interaction with JAK2 phosphorylated
on tyrosine residues; the N-terminus provides a low-affinity binding to
JAK2 independent of JAK2 phosphorylation. Isoform 3 interacts via its
SH2 domain with JAK2. Isoform 1 interacts via its SH2 domain with INSR;
the interaction requires receptor activation. Isoform 3 interacts via
its SH2 domain with INSR; the interaction requires receptor activation
and requires INSR phosphorylation at 'Tyr-1175'. Isoform 1 interacts
with IGF1R; the interaction requires receptor activation. Isoform 2
interacts via its SH2 domain with FGFR3; the interaction requires FGFR3
'Tyr-719' and 'Tyr-755'. Isoform 2 interacts with RET; the interaction
requires RET kinase activity and RET 'Tyr-982'. Isoform 2 interacts
with RAC1. Isoform 2 interacts with PDGFRA and/or PDGFRB; the
interaction requires receptor activation. Interacts with ISR1 and ISR2.
Isoform 3 is probably part of a complex consisting of INSR, ISR1 and
SH2B1. Probably part of a ternary complex consisting of SH2B1, JAK2 and
ISR1 or ISR2. May interact with FCER1G (By similarity). Interacts (via
SH2 domain) with NTRK1 (phosphorylated) (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q91ZM2; Q62120: Jak2; NbExp=3; IntAct=EBI-7178606, EBI-646604;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000305}.
Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the
cytoplasm. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Alpha;
IsoId=Q91ZM2-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q91ZM2-2; Sequence=VSP_032032;
Name=3; Synonyms=Gamma;
IsoId=Q91ZM2-3; Sequence=VSP_032033;
Name=4; Synonyms=Delta;
IsoId=Q91ZM2-4; Sequence=VSP_032034;
Name=5;
IsoId=Q91ZM2-5; Sequence=VSP_032029, VSP_032031;
Name=6; Synonyms=Sh2bpsm1 gamma;
IsoId=Q91ZM2-6; Sequence=VSP_032030, VSP_032033;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver,
brain and heart. Isoform 3 is widely expressed.
{ECO:0000269|PubMed:10594240, ECO:0000269|PubMed:9498552}.
-!- PTM: Phosphorylated on tyrosine residues in response to IGF-I and PDGF
stimulation. {ECO:0000269|PubMed:11502739}.
-!- SIMILARITY: Belongs to the SH2B adapter family. {ECO:0000305}.
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EMBL; AF020526; AAC33414.1; -; mRNA.
EMBL; AF380422; AAL07566.1; -; mRNA.
EMBL; AF074329; AAD41655.1; -; mRNA.
EMBL; AF421138; AAL16069.1; -; mRNA.
EMBL; AF421139; AAL16070.1; -; mRNA.
EMBL; AK168439; BAE40344.1; -; mRNA.
EMBL; AK170444; BAE41802.1; -; mRNA.
EMBL; BC011422; AAH11422.1; -; mRNA.
EMBL; BC051978; AAH51978.1; -; mRNA.
EMBL; AF036355; AAC39955.2; -; mRNA.
CCDS; CCDS40126.1; -. [Q91ZM2-3]
CCDS; CCDS85410.1; -. [Q91ZM2-4]
CCDS; CCDS85411.1; -. [Q91ZM2-1]
CCDS; CCDS85412.1; -. [Q91ZM2-2]
PIR; JC5886; JC5886.
RefSeq; NP_001074928.1; NM_001081459.2. [Q91ZM2-2]
RefSeq; NP_001276467.1; NM_001289538.1. [Q91ZM2-1]
RefSeq; NP_001276468.1; NM_001289539.1. [Q91ZM2-2]
RefSeq; NP_001276469.1; NM_001289540.1. [Q91ZM2-2]
RefSeq; NP_001276470.1; NM_001289541.1. [Q91ZM2-4]
RefSeq; NP_001276471.1; NM_001289542.1. [Q91ZM2-4]
RefSeq; NP_035493.2; NM_011363.3. [Q91ZM2-3]
RefSeq; XP_006507541.1; XM_006507478.3. [Q91ZM2-1]
RefSeq; XP_006507543.1; XM_006507480.3. [Q91ZM2-1]
RefSeq; XP_006507544.1; XM_006507481.3. [Q91ZM2-1]
RefSeq; XP_006507545.1; XM_006507482.1. [Q91ZM2-1]
RefSeq; XP_006507548.1; XM_006507485.3. [Q91ZM2-3]
RefSeq; XP_006507550.1; XM_006507487.3. [Q91ZM2-2]
PDB; 2HDV; X-ray; 2.00 A; A/B=519-627.
PDB; 2HDX; X-ray; 2.35 A; A/B/C/D/E/F=519-627.
PDBsum; 2HDV; -.
PDBsum; 2HDX; -.
SMR; Q91ZM2; -.
BioGRID; 203201; 2.
IntAct; Q91ZM2; 4.
MINT; Q91ZM2; -.
STRING; 10090.ENSMUSP00000032978; -.
iPTMnet; Q91ZM2; -.
PhosphoSitePlus; Q91ZM2; -.
jPOST; Q91ZM2; -.
PaxDb; Q91ZM2; -.
PeptideAtlas; Q91ZM2; -.
PRIDE; Q91ZM2; -.
Antibodypedia; 26583; 277 antibodies.
Ensembl; ENSMUST00000032978; ENSMUSP00000032978; ENSMUSG00000030733. [Q91ZM2-3]
Ensembl; ENSMUST00000205340; ENSMUSP00000145953; ENSMUSG00000030733. [Q91ZM2-2]
Ensembl; ENSMUST00000205440; ENSMUSP00000145554; ENSMUSG00000030733. [Q91ZM2-2]
Ensembl; ENSMUST00000205497; ENSMUSP00000145842; ENSMUSG00000030733. [Q91ZM2-4]
Ensembl; ENSMUST00000205733; ENSMUSP00000145754; ENSMUSG00000030733. [Q91ZM2-1]
Ensembl; ENSMUST00000205889; ENSMUSP00000146282; ENSMUSG00000030733. [Q91ZM2-4]
Ensembl; ENSMUST00000206664; ENSMUSP00000146121; ENSMUSG00000030733. [Q91ZM2-5]
GeneID; 20399; -.
KEGG; mmu:20399; -.
UCSC; uc009jrh.2; mouse. [Q91ZM2-2]
UCSC; uc009jrj.2; mouse. [Q91ZM2-4]
UCSC; uc009jrk.2; mouse. [Q91ZM2-3]
UCSC; uc009jrm.2; mouse. [Q91ZM2-1]
CTD; 25970; -.
MGI; MGI:1201407; Sh2b1.
eggNOG; ENOG410IMWK; Eukaryota.
eggNOG; ENOG41102PH; LUCA.
GeneTree; ENSGT00950000183191; -.
HOGENOM; CLU_014885_4_0_1; -.
InParanoid; Q91ZM2; -.
KO; K12459; -.
OMA; SSTLMPF; -.
OrthoDB; 556279at2759; -.
PhylomeDB; Q91ZM2; -.
TreeFam; TF323184; -.
Reactome; R-MMU-1170546; Prolactin receptor signaling.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
BioGRID-ORCS; 20399; 4 hits in 12 CRISPR screens.
ChiTaRS; Sh2b1; mouse.
EvolutionaryTrace; Q91ZM2; -.
PRO; PR:Q91ZM2; -.
Proteomes; UP000000589; Chromosome 7.
RNAct; Q91ZM2; protein.
Bgee; ENSMUSG00000030733; Expressed in molar tooth and 279 other tissues.
Genevisible; Q91ZM2; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0001726; C:ruffle; TAS:MGI.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
GO; GO:2000278; P:regulation of DNA biosynthetic process; IMP:UniProtKB.
CDD; cd10346; SH2_SH2B_family; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
IDEAL; IID50098; -.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR015012; Phe_ZIP.
InterPro; IPR036290; Phe_ZIP_sf.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR030523; SH2B.
InterPro; IPR030521; SH2B1.
InterPro; IPR035057; SH2B1_SH2.
PANTHER; PTHR10872; PTHR10872; 1.
PANTHER; PTHR10872:SF3; PTHR10872:SF3; 1.
Pfam; PF00169; PH; 1.
Pfam; PF08916; Phe_ZIP; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00233; PH; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF109805; SSF109805; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cytoplasm; Membrane; Methylation;
Nucleus; Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1..756
/note="SH2B adapter protein 1"
/id="PRO_0000323594"
DOMAIN 267..376
/note="PH"
DOMAIN 527..625
/note="SH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
REGION 1..555
/note="Interaction with JAK2 (low-affinity binding;
independent of JAK2 phosphorylation)"
/evidence="ECO:0000250"
REGION 24..85
/note="Required for self-association"
/evidence="ECO:0000250"
REGION 85..196
/note="Interaction with RAC1"
/evidence="ECO:0000250"
REGION 100..243
/note="Required for NGF signaling"
/evidence="ECO:0000250"
REGION 224..233
/note="Required for nuclear localization"
/evidence="ECO:0000250"
MOD_RES 88
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 96
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 270
/note="Omega-N-methylarginine"
/evidence="ECO:0000244|PubMed:24129315"
MOD_RES 417
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 420
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 439
/note="Phosphotyrosine; by JAK1, JAK2 and PDGFR"
/evidence="ECO:0000250|UniProtKB:Q62985"
MOD_RES 494
/note="Phosphotyrosine; by JAK1, JAK2"
/evidence="ECO:0000250|UniProtKB:Q62985"
VAR_SEQ 437..443
/note="GAYGGLS -> AVDSEKT (in isoform 5)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_032029"
VAR_SEQ 441..460
/note="Missing (in isoform 6)"
/evidence="ECO:0000303|PubMed:10594240"
/id="VSP_032030"
VAR_SEQ 444..756
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_032031"
VAR_SEQ 632..756
/note="ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAAAKERQEKEKAG
SGGVQEELVPVAELVPMVELEEAIAPGTEAQGGAGSSGDLEVSLMVQLQQLPLGGNGEE
GGHPRAINNQYSFV -> GREQAGSHAGVCEGDRCYPDASSTLLPFGASDCVTEHLP
(in isoform 2)"
/evidence="ECO:0000303|PubMed:11502739,
ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9498552"
/id="VSP_032032"
VAR_SEQ 632..756
/note="ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAAAKERQEKEKAG
SGGVQEELVPVAELVPMVELEEAIAPGTEAQGGAGSSGDLEVSLMVQLQQLPLGGNGEE
GGHPRAINNQYSFV -> GEQSRSAGEEVPVHPRSEAGSRLGAMQGCARATDATPMPPP
PSCPSERVTV (in isoform 3 and isoform 6)"
/evidence="ECO:0000303|PubMed:10594240,
ECO:0000303|PubMed:11502739, ECO:0000303|PubMed:16141072"
/id="VSP_032033"
VAR_SEQ 632..756
/note="ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAAAKERQEKEKAG
SGGVQEELVPVAELVPMVELEEAIAPGTEAQGGAGSSGDLEVSLMVQLQQLPLGGNGEE
GGHPRAINNQYSFV -> GEQSRSAGEEVPVHPRSENGAPPVTQPSPLNPLHGQIPHIL
GQKRRRGRQKLRQPQPQQPKRGKRKRKRAVEGSRKSWSPWLSWSPWLNWKRP (in
isoform 4)"
/evidence="ECO:0000303|PubMed:11502739,
ECO:0000303|PubMed:15489334"
/id="VSP_032034"
CONFLICT 172
/note="W -> C (in Ref. 2; AAD41655)"
/evidence="ECO:0000305"
CONFLICT 399
/note="F -> L (in Ref. 5; AAH11422)"
/evidence="ECO:0000305"
CONFLICT 564
/note="Y -> C (in Ref. 2; AAD41655)"
/evidence="ECO:0000305"
HELIX 522..524
/evidence="ECO:0000244|PDB:2HDV"
STRAND 528..531
/evidence="ECO:0000244|PDB:2HDV"
HELIX 534..542
/evidence="ECO:0000244|PDB:2HDV"
HELIX 545..548
/evidence="ECO:0000244|PDB:2HDV"
STRAND 551..556
/evidence="ECO:0000244|PDB:2HDV"
STRAND 558..560
/evidence="ECO:0000244|PDB:2HDX"
STRAND 563..570
/evidence="ECO:0000244|PDB:2HDV"
STRAND 573..581
/evidence="ECO:0000244|PDB:2HDV"
STRAND 587..589
/evidence="ECO:0000244|PDB:2HDV"
STRAND 592..596
/evidence="ECO:0000244|PDB:2HDV"
HELIX 597..604
/evidence="ECO:0000244|PDB:2HDV"
TURN 612..616
/evidence="ECO:0000244|PDB:2HDX"
SEQUENCE 756 AA; 79625 MW; 388BDC44267E6DE8 CRC64;
MNGAPSPEDG VFPSPPALPP PPPPSWQEFC ESHARAAALD LARRFRLYLA SHPQYAEPGA
EAAFSGRFAE LFLQHFEAEV ARASGSLSPP VLAPLSPGVE IPPSHDLSLE SCRVGGPLAV
LGPSRSSEDL AGPLPSSVPS STTSSKPKLK KRFSLRSVGR SVRGSVRGIL QWRGAVDSPS
QAGPLETTSG PPVLGGNSNS NSSGGAGTVG RALANDGTSP GERWTHRFER LRLSRGGGTL
KDGAGMIQRE ELLSFMGAEE AAPDPAGVGR GGGAAGLTSG GGGQPQWQKC RLLLRSEGEG
GGGSRLEFFV PPKASRPRLS IPCSTITDVR TATALEMPDR ENTFVVKVEG PSEYILETSD
ALHVKAWVSD IQECLSPGPC PAISPRPMTL PLAPGTSFFT KDNTDSLELP CLNHSESLPS
QDLLLGPSES NDRLSQGAYG GLSDRPSASF SPSSASIAAS HFDSMELLPP ELPPRIPIEE
GPPAGTVHPL STPYPPLDTP EAATGSFLFQ GESEGGEGDQ PLSGYPWFHG MLSRLKAAQL
VLEGGTGSHG VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM
LEHFRVHPIP LESGGSSDVV LVSYVPSQRQ QERSTSRDPA QPSEPPPWTD PPHPGAEEAS
GAPEVAAATA AAAKERQEKE KAGSGGVQEE LVPVAELVPM VELEEAIAPG TEAQGGAGSS
GDLEVSLMVQ LQQLPLGGNG EEGGHPRAIN NQYSFV


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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP73: G Protein Signaling Pathways
WP2292: Chemokine signaling pathway
WP813: G Protein Signaling Pathways
WP211: BMP signaling pathway
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP2032: TSH signaling pathway
WP1049: G Protein Signaling Pathways
WP2272: Pathogenic Escherichia coli infection
WP232: G Protein Signaling Pathways
WP2203: TSLP Signaling Pathway
WP35: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways
WP116: Hedgehog Signaling Pathway
WP319: IL-3 Signaling Pathway
WP1313: Insulin Signaling
WP480: T Cell Receptor Signaling Pathway
WP1381: G13 Signaling Pathway
WP1673: Naphthalene and anthracene degradation
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1912: Signaling by GPCR
WP10: IL-9 Signaling Pathway
WP918: p38 MAPK Signaling Pathway (BioCarta)
WP998: MAPK signaling pathway

Related Genes :
[Sh2b1 Sh2bpsm1] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[SH2B1 KIAA1299 SH2B] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B)
[Sh2b1 Sh2-b Sh2bpsm1] SH2B adapter protein 1 (FceRI gamma-chain-interacting protein SH2-B) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[Sh2d1b Eat2 Eat2a Sh2d1b1] SH2 domain-containing protein 1B (EWS/FLI1-activated transcript 2) (EAT-2)
[SH2D1A DSHP SAP] SH2 domain-containing protein 1A (Duncan disease SH2-protein) (Signaling lymphocytic activation molecule-associated protein) (SLAM-associated protein) (T-cell signal transduction molecule SAP)
[GRB2 ASH] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[SH2D2A SCAP TSAD VRAP] SH2 domain-containing protein 2A (SH2 domain-containing adapter protein) (T cell-specific adapter protein) (TSAd) (VEGF receptor-associated protein)
[BCAR3 NSP2 SH2D3B UNQ271/PRO308] Breast cancer anti-estrogen resistance protein 3 (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B)
[Inpp5d 7a33 Ship Ship1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (Phosphatidylinositol-4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship)
[BLNK BASH SLP65] B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (SLP-65)
[SHC1 SHC SHCA] SHC-transforming protein 1 (SHC-transforming protein 3) (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[Grb2] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2)
[Grb2 Ash] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[Shc1 Shc ShcA] SHC-transforming protein 1 (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[INPPL1 SHIP2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[Shc1] SHC-transforming protein 1 (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[INPP5D SHIP SHIP1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship) (hp51CN)
[Inpp5d Ship Ship1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Phosphatidylinositol-4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1)
[SHB] SH2 domain-containing adapter protein B
[Socs3 Cis3 Cish3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (Protein EF-10)
[SHC3 NSHC SHCC] SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (Protein Rai) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3)
[SOCS3 CIS3 SSI3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (STAT-induced STAT inhibitor 3) (SSI-3)
[Shb] SH2 domain-containing adapter protein B
[Socs3 Cish3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3)
[Inppl1 Ship2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (AblSH3-binding protein) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[Inppl1 Ship2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[Blnk Bash Ly57 Slp65] B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Lymphocyte antigen 57) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (Slp-65)
[Ctr9 Kiaa0155 Sh2bp1] RNA polymerase-associated protein CTR9 homolog (SH2 domain-binding protein 1) (Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa) (TPR-containing, SH2-binding phosphoprotein of 150 kDa) (p150TSP)
[INPPL1 SHIP2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[NCK1 NCK] Cytoplasmic protein NCK1 (NCK adaptor protein 1) (Nck-1) (SH2/SH3 adaptor protein NCK-alpha)

Bibliography :